Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform  

UniProtKB / Swiss-Prot ID :  PP2AA_HUMAN

Gene Name (Synonyms) : 
PPP2CA  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus. Chromosome, centromere. Cytoplasm, cytoskeleton, spindle pole. Note=In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles. Centromeric localization requires the presenc 

Protein Function :  PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Cooperates with SGOL2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I (By similarity). Can dephosphorylate SV40 large T antigen and p53/TP53. Dephosphorylates SV40 large T antigen, preferentially on serine residues 120, 123, 677, and perhaps 679. The C subunit was most active, followed by the AC form, which was more active than the ABC form, and activity of all three forms was strongly stimulated by manganese, and to a lesser extent by magnesium. Dephosphorylation by the AC form, but not C or ABC form is inhibited by small T antigen. Activates RAF1 by dephosphorylating it at 'Ser-259'. 

Protein Sequence MDEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVHGQFHDLMELFR...
Predicted Secondary Structure CCCCCCCCCHHHHHHHHHHCCCCCHHHHHHHHHHHHHHHHCCCCCEECCCCEEEEECCCCCHHHHHHHHH...
Protein Variant
LocationDescription
52V -> A (in dbSNP:rs11552681). VAR_051735
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
1N-acetylmethionine.----MDEKV
----CCCCC
15.76UniProtKB
Link-
4N6-acetyllysine-MDEKVFTK
-CCCCCCCC
38.08HPRD
Link
4N6-acetyllysine-MDEKVFTK
-CCCCCCCC
38.08Phosphositeplus
Link
4N6-acetyllysine.-MDEKVFTK
-CCCCCCCC
38.08UniProtKB
Link
8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KVFTKELDQ
CCCCCCHHH
44.83Phosphositeplus
Link
21Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LNECKQLSE
HHHCCCCCH
48.36Phosphositeplus
Link
29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ESQVKSLCE
HHHHHHHHH
30.03Phosphositeplus
Link
34Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SLCEKAKEI
HHHHHHHHH
64.86Phosphositeplus
Link
41Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EILTKESNV
HHHHCCCCC
56.55Phosphositeplus
Link
74Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RIGGKSPDT
HHHCCCCCC
54.31Phosphositeplus
Link
136Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ECLRKYGNA
HHHHHCCCH
44.56Phosphositeplus
Link
248PhosphotyrosineVMEGYNWCH
HHHHHHHHH
7.68Phosphositeplus
Link
265PhosphotyrosineSAPNYCYRC
ECCCHHHCC
6.98Phosphositeplus
Link
266S-nitrosocysteineAPNYCYRCG
CCCHHHCCC
1.88dbSNO
Link
283Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DDTLKYSFL
ECCCCEEEE
40.72Phosphositeplus
Link
284PhosphotyrosineDTLKYSFLQ
CCCCEEEEE
14.04Phosphositeplus
Link
304PhosphothreonineVTRRTPDYF
CCCCCCCCC
19.74PhosphoELM
Link
304PhosphothreonineVTRRTPDYF
CCCCCCCCC
19.74Phosphositeplus
Link
307PhosphotyrosineRTPDYFL
CCCCCCC
14.16PhosphoELM
Link
307PhosphotyrosineRTPDYFL
CCCCCCC
14.16Phosphositeplus
Link
307Phosphotyrosine.RTPDYFL
CCCCCCC
14.16UniProtKB
Link
309Leucine methyl ester.PDYFL
CCCCC
5.81UniProtKB
Link
309N-methylleucinePDYFL
CCCCC
5.81Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
BCL2_HUMANdephosphorylation reactionMINT-51443MINT15225643
AKT1_HUMANphysical interactionMINT-74931MINT16044149
AKT1_HUMANphysical interactionMINT-74941MINT16044149
IEX1_HUMANphysical interactionMINT-2835686MINT16456541
RT26_HUMANphysical interactionMINT-65395MINT16169070
Q9NSU0_HUMANphysical interactionMINT-65632MINT16169070
PTN_HUMANphysical interactionEBI-729147
intact16169070
TRP13_HUMANphysical interactionEBI-753586
intact16189514
KS6B1_HUMANENSP00000231504STRING
AKT1_HUMANENSP00000231504STRING
CCNG2_HUMANENSP00000231504STRING
2ABA_HUMANENSP00000231504STRING
4EBP1_HUMANENSP00000231504STRING
IGBP1_HUMANENSP00000231504STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00163Vitamin E
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-4, AND MASSSPECTROMETRY.
Methylation
ReferencePubMed
"The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo.";
Favre B., Zolnierowicz S., Turowski P., Hemmings B.A.;
J. Biol. Chem. 269:16311-16317(1994).
Cited for: METHYLATION AT LEU-309.
Phosphorylation
ReferencePubMed
"Protein phosphatase 2A dephosphorylates simian virus 40 large Tantigen specifically at residues involved in regulation of DNA-bindingactivity.";
Scheidtmann K.H., Virshup D.M., Kelly T.J.;
J. Virol. 65:2098-2101(1991).
Cited for: SITES OF DEPHOSPHORYLATION AT SV40 LARGE-T ANTIGEN.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures